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3.1.1.4: phospholipase A2

This is an abbreviated version!
For detailed information about phospholipase A2, go to the full flat file.

Word Map on EC 3.1.1.4

Reaction

phosphatidylcholine
+
H2O
=
1-acylglycerophosphocholine
 +
a carboxylate

Synonyms

1-CysPrx, 1-cysteine peroxiredoxin, 14 kDa phospholipase A2, A2-IIA, Acanmyotoxin-1, acidic Asp49 phospholipase A2, acidic Ca2+-independent phospholipase A2, acidic phospholipase A2, ACS, adiponutrin, AdPLA, Agkistrotoxin, AgkTx-II, aiPLA2, alpha-type phospholipase A2, amdI1, Ammodytin I2, ammodytoxin A, APLA, APP-D-49, Arg49 phospholipase A2, Arg49 phospholipase A2 homologue, Asp49 basic myotoxic PLA2, Asp49 PLA2, Asp49-PLA2, ASPLA1, ASPLA10, ASPLA11, ASPLA12, ASPLA13, ASPLA14, ASPLA15, ASPLA16, ASPLA17, ASPLA2, ASPLA3, ASPLA4, ASPLA5, ASPLA6, ASPLA7, ASPLA8, ASPLA9, Ats-PLA2-alpha, AtsPLA2-alpha, AtsPLA2-gamma, ATX, BaltPLA2, basic Asp49 PLA2, Basic protein I/II, BaTX, BinTx-I, BinTx-II, BJ-PLA2, Bj-V, BJUPLA2, Bothropstoxin-I, BPI/BPII, BthTX, BthTX-1, BthTX-I, BthTX-II, bvPLA2, Ca+2-independent PLA2, Ca2+ independent PLA2, Ca2+-independent iPLA2, Ca2+-independent phospholipase A2, Ca2+-independent PLA2, CaI-PLA2, calcium-d-independent cytosolic PLA2, calcium-dependent cytosolic PLA2, calcium-independent group VIA iPLA2, calcium-independent phospholipase A2, Caudoxin, Cdt PLA2, class XIB phospholipase A2, ColTx-I, cPLA2, cPLA2 alpha, cPLA2-alpha, cPLA2-gamma, cPLA2-zeta2, cPLA2alpha, cPLA2beta, cPLA2delta, cPLA2epsilon, cPLA2zeta, cPm09, Cr-IV 1, Cro, crotapotin, crotoxin, CTX, cytoplasmic phospholipase A2, cytosolic calcium-dependent PLA2, cytosolic cPLA2, cytosolic gIVaPLA2, cytosolic group IVA cPLA2, cytosolic group IVa phospholipase A2, cytosolic phospholipase A2, cytosolic phospholipase A2 alpha, cytosolic phospholipase A2-alpha, cytosolic phospholipase A2alpha, cytosolic PLA2, cytotoxin ExoU, Daboxin P, DrK-aI, DrK-aII, DrK-bI, DrK-bII, DrPLA2, DsM-bI, DsM-S1, Enhancing factor, exoenzyme U, ExoU, ExoU-specific PLA2, GIA cobra venom PLA2, GIIA, GIIA PLA2, GIIA sPLA2, GIIC sPLA2, GIID, GIID sPLA2, GIIE, GIIE sPLA2, GIIF, GIIF sPLA2, GIII sPLA2, GIIIsPLA2, GIVA, GIVA cPLA2, GIVA phospholipase A2, GIVA PLA2, GIVD cPLA2delta, GIVF, Gln49-PLA2, group IA PLA2, Group IB phospholipase A2, group IB PLA2, group II snake venom phospholipase A2, Group IIA phospholipase A2, group IIA PLA2, group IIA secretory phospholipase A2, group IIA secretory PLA2, group IID secretory phospholipase A2, group III Glu62-phospholipase A2, group III PLA2, group III sPLA2, group IV cPLA2, group IVA cPLA2, group IVA cytosolic phospholipase A2, group IVA phospholipase A2, group IVA PLA2, group IVB phospholipase A2, Group V phospholipase A2, group V secreted phospholipase A2, Group VI phospholipase A2, Group VIA Ankyrin-1, Group VIA Ankyrin-2, group VIA calcium-independent phospholipase A, group VIA cPLA2, group VIA phospholipase A2, Group VIA PLA2, Group VIA-3, group X secreted phospholipase A2, GS2, GV sPLA2, GVI PLA2, GVIA, GVIA iPLA2, GVIA PLA2, GVIA-iPLA2, GVIIA PLA2, GX, GX sPLA2, GXII sPLA2, GXIIA, GXIII sPLA2, hGX sPLA2, hIBPLA2, hIIAPLA2, human group IB PLA2, human group IIA phospholipase A2, IB PLA2, immune-associated phospholipase A2, imperatoxin, intercro, IPLA-1, iPLA2, iPLA2-gamma, jerdoxin, lecithinase A, lipoprotein associated phospholipase A2, lipoprotein-associated phospholipase A2, lipoprotein-associated PLA2, LLPL, LM-PLA2-I, LM-PLA2-II, LmTX-I, LmTX-II, Lp-PLA2, Lpla2, Lys49 phospholipase A2 homologue, Lys49-phospholipase A2 homologue, Lys49-PLA2, lysophospholipase, lysosomal phospholipase A2, lysosomal PLA2, mAoPlaA, marine snail digestive phospholipase A2, megacin A-216, MiDCA1, milleporin-1, MjTX-II, More, MP-III 4R, mSDPL, MsPLA2-I, Muscarinic inhibitor, mycotoxin II, myotoxic Asp49-phospholipase A2, myotoxic phospholipase A2, Myotoxin, myotoxin I, NAJPLA-2A, NAJPLA-2B, NAJPLA-2C, natratoxin, neuropathy target esterase, neutral anticoagulant secretory phospholipase A2, Nigexine, NK-PLA2-I, NK-PLA2-II, NN-X-PLA2, NN-XI-PLA2, NN-XIa-PLA2, NND-IV-PLA2, Non-pancreatic secretory phospholipase A2, Notechis 11'2, Notexin, notexinII-1, NPLA, NPS-PLA2, OHV A-PLA2, OHV-APLA2, OPLA2, PAF acetyl hydrolase/oxidized lipid LpPLA2, PAF-AH, pancreatic phospholipase A2, pancreatic-type PLA2, patatin, peroxiredoxin 6, pgPLA 1a/pgPLA 2a, PhlA, phosphatidase, phosphatide 2-acylhydrolase, phosphatidolipase, Phosphatidylcholine 2-acylhydrolase, Phosphatidylcholine 2-acylhydrolase GIIC, Phosphatidylcholine 2-acylhydrolase GIID, Phosphatidylcholine 2-acylhydrolase GIIE, Phosphatidylcholine 2-acylhydrolase GIIF, Phosphatidylcholine 2-acylhydrolase GIII, Phosphatidylcholine 2-acylhydrolase GX, Phosphatidylcholine 2-acylhydrolase GXII, Phosphatidylcholine 2-acylhydrolase GXIII, phospholipase A, phospholipase A2, phospholipase A2 D49, phospholipase A2 gamma, Phospholipase A2 inhibitor, phospholipase A2 neurotoxin, phospholipase A2 PA-11, phospholipase A2alpha, phospholipase A2IValpha, phospholipase A2s, phospholipin, pkP5, Pla, PLA1, PLA2, PLA2 CM2, PLA2 neurotoxin, PLA2-10, PLA2-1B, PLA2-2A, PLA2-2C, PLA2-H, PLA2-I, PLA2-L, PLA2-V, PLA2-VI, PLA2-VII, PLA2alpha, PLA2G1B, PLA2G2D, Pla2g4a, Pla2g4b, PLA2G4C, PLA2G4D, PLA2G6, PLA2IID, PLA2III, PLA2IValpha, PLA2s, platelet activating factor acetyl hydrolase, platelet activating factor acetyl hydrolase/oxidized lipid LpPLA2, platelet-activating factor acetylhydrolase, platlet-activating factor acetylhydrolase, plpA, ppPLA2, Prdx6, promutoxin, PrTX-1, PrTX-I, PrTX-III, Pt-PLA1, Pt-PLA2, R49 PLA2, RVV acidic PLA2-I, RVV-7, RVVA-PLA2-I, SCO1048 protein, Scol/Pla, secreted group IID phospholipase A2, secreted human phospholipase A2, secreted phospholipase A2, secreted phospholipaseA2 neurotoxin, secreted phospholipases A2, secreted PLA2, secreted sPLA2, secretory Ca2+-dependent PLA2, secretory phospholipase, secretory phospholipase A2, secretory phospholipase A2 group IIA, secretory phospholipase A2 type IB, secretory phospholipase A2 type IIA, secretory phospholipase A2-alpha, secretory PLA2s, Secretory-type PLA, stroma-associated homolog, snake presynoptic phospholipase A2 neurotoxin, SPAN, specific phospholipase A2, sPLA(2), sPLA(2)-IID, sPLA(2)-IIE, sPLA(2)-IIF, sPLA-V, sPLA2, sPLA2 GIB, sPLA2 GIIA, sPLA2 IB, sPLA2 type IIA, sPLA2(IIA), sPLA2-IB, sPLA2-IIA, sPLA2-IID, sPLA2-IIE, sPLA2-IIF, sPLA2-V, sPLA2-X, sPLA2:, sPLA2IB2, svPLA2, taipoxin, textilotoxin, thrombin inhibitor from Naja haje, TI-Nh, TMV-K49, toxin I, Toxin VI, Toxin VI:5, TPP, trimorphin, TTS-2.2, Tx-1, TX-I, type III cytotoxin, type VIIA PLA2, zhaoermiatoxin

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.4 phospholipase A2

Engineering

Engineering on EC 3.1.1.4 - phospholipase A2

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H75A/D76N
the secretory phospholipase A2 defect in H75A/D76N severely impairs adeno-associated virus' infectivity
R238A
the activity of the R238A mutant isx0140% of that of wild type enzyme. The growth of the strain overexpressing R238A is similar to that of the strain overexpressing wild type AoPlaA, presumably because the residual activity of R238A is sufficient to cause growth retardation
S266A
mutation abolishes the enzyme activity
D49K
site-directed mutagenesis, the tertiary structures of the active site mutant is similar to that of the trigonal recombinant enzyme, but the mutant lacks a Ca2+ in the active site. Molecular-dynamics simulation, proton transfer is not possible from the catalytic water to the mutated residue
D49N
site-directed mutagenesis, the tertiary structures of the active site mutant is similar to that of the trigonal recombinant enzyme, but the mutant lacks a Ca2+ in the active site. Molecular-dynamics simulation, proton transfer is not possible from the catalytic water to the mutated residue
H48N
site-directed mutagenesis, the tertiary structures of the active site mutant is similar to that of the trigonal recombinant enzyme. Molecular-dynamics simulation, proton transfer is not possible from the catalytic water to the mutated residue
K53M/K56M/K120M
crystal structure is similar to wild-type enzyme
A206K
-
site-directed mutagenesis
C47S
-
the mutation results in the loss of peroxidase activity but acidic Ca2+-independent phospholipase A2 activity remains intact
D43N
-
site-directed mutagenesis
D47E
-
site-directed mutagenesis, inactive mutant
D47K
-
site-directed mutagenesis, inactive mutant
DELTAK57/R58
suramin affinity is significantly increased
E89K
-
surface charge replacements, mutant shows increased activitiy at neutral pH, 2.3 times that of the wild-type enzyme at pH 7
F5W
-
site-directed mutagenesis, mutation of the substrate binding pocket leads to reduced enzyme activity, the inhibitory effect of the F5W mutation results from the high affinity of Trp for the membrane-water interface
G30S
mutant shows 50% reduced hydrolytic activity against dioleoylphosphatidylcholine:dioleoylphosphatidylcholine liposome membranes and reduced killing of Gram-negative bacteria
H46N
-
site-directed mutagenesis, inactive mutant
H48A
mutation has a serious effect on the structural integrity of the enzyme
H48N
0.2% catalytic activity
K116A
suramin affinity is increased, inhibitory effect of suramin in relation to wild-type protein is enhanced
K123A
suramin affinity is significantly reduced, inhibitory effect of suramin in relation to wild-type protein is reduced
K15A
suramin affinity is significantly reduced, inhibitory effect of suramin in relation to wild-type protein is reduced
K488N/K543N/K544N
-
site-directed mutagenesis, the mutant shows 2fold increased activity compared to the wild-type enzyme
K554A/D555A/K556A
to crystallize apo-cPLA2d, three surface mutations (K554A, D555A, and K556A) are introduced to decrease surface entropy
M20L
-
according the gapped-duplex method, using amber selection
M8L
-
according the gapped-duplex method, using amber selection
N273
mutation in potential N-glycosylation site, reduction in catalytic activity, mutant is recovered in the soluble fraction
N289
mutation in potential N-glycosylation site, reduction in catalytic activity, mutant is recovered in the soluble fraction
N398
mutation in potential N-glycosylation site, reduction in catalytic activity, mutant is recovered in the soluble fraction
N99
mutation in potential N-glycosylation site, marked reduction in catalytic activity, mutant is mostly retained in the membrane fraction
N99/N273/N289/N398
mutation in all potential glycosylation sites, loss of catalyic activity
R100E
-
surface charge replacements, mutant shows increased activitiy at neutral pH, 2.8, and times that of the wild-type enzyme at pH 7
R42E
-
surface charge replacements, mutant shows increased activitiy at neutral pH, 2.3times that of the wild-type enzyme at pH 7
R54A
suramin affinity is significantly reduced, inhibitory effect of suramin in relation to wild-type protein is reduced
R58A
inhibitory effect of suramin in relation to wild-type protein is reduced
R7A
inhibitory effect of suramin in relation to wild-type protein is reduced
S32A
-
the mutation abolishes acidic Ca2+-independent phospholipase A2 activity while the peroxidase activity remained unaffected
S505A
S505A/S727A
-
site-directed mutagenesis
S505A/S727A/S515A
-
site-directed mutagenesis
S505E
S505E/S727A
-
site-directed mutagenesis
S515A
-
site-directed mutagenesis
S727A
S727E
-
mutation of the phosphorylation site Ser727 leading to a phosphorylation-mimicking mutant, the mutant shows unaltered enzyme activity compared to the wild-type enzyme
S727T
-
mutation of the phosphorylation site Ser727, S727T is as potently inhibited by annexin A2-p11 heterotetramer as the wild type cPLA2alpha, the mutant shows unaltered enzyme activity compared to the wild-type enzyme
T177A
-
the mutation of Thr177 abolishes protein phosphorylation and the increase in MAP kinase-mediated activity of the mutant
T177E
-
the mutation of Thr177 abolishes protein phosphorylation and the increase in MAP kinase-mediated activity of the mutant
Y50F
-
site-directed mutagenesis, inactive mutant
D49K
-
5% enzymatic activity
H48N
-
no enzymatic activity
H48Q
-
mutant with very weak enzymatic activity
D97N
-
reduced activity of acidic secretory isoforms PLA2-1 and PLA2-2
H47A
-
no activity of acidic secretory isoforms PLA2-1 and PLA2-2
H47R
-
no activity of acidic secretory isoforms PLA2-1 and PLA2-2
N1M
site-directed mutagenesis, the mutants with an extra Met before Asn1 or substituting Asn1 with Met still retain approximately 40.9% and 82.9% membrane-damaging activity of the native enzyme, respectively. Mutations on the N-terminal region do not greatly affect the Ca2+-binding ability but cause a precipitous drop in PLA2 activity. The gross conformation of the mutant is altered compared to the native enzyme, overview. The enzymatic activity of the mutant is approximately 5.3% of that of native PLA2
K49R
catalytically inactive enzyme, the orientation of the Arg49 side chain results in a similar binding mode to that observed in the Lys49 PLA2s
A384G
complete loss of cytotoxicity
E464D
54% of wild-type cytotoxicity
I609N
mutant is relatively insensitive to activation by ubiquitin, but with excess ubiquitin it is synergistically activated by phosphatidylinositol 4,5-bisphosphate
K359N
77% of wild-type cytotoxicity
K395R
110% of wild-type cytotoxicity
N369D
110% of wild-type cytotoxicity
S142A
catalytically inactive
V423F
50% of wild-type cytotoxicity
V462F
37% of wild-type cytotoxicity
C651A
-
catalytic activity similar to wild-type, inactivation by (6E)-6-(bromomethylene)-3-(1-naphthyl)tetrahydro-2H-pyran-2-one requires higher concentrations than for wild-type
D192A
-
no enzymatic activity
H175N
-
10% of wild-type activity
H288N
-
as active as wild-type enzyme
K17A
-
no enzymatic activity
S10C
-
29% of wild-type activity
S10T
-
25% of wild-type activity
S234C
-
no enzymatic activity
S234T
-
no enzymatic activity
S54A
-
no enzymatic activity
S54C
-
1% of wild-type activity
S54T
-
no enzymatic activity
A12T/H15D/M20L/E71N
catalytic activity similar to wild-type
F63V
-
-
Y52F
-
-
Y73F
-
-
additional information